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Unification of lower and upper critical solution temperature phase behavior of globular protein solutions in the presence of multivalent cations

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Abstract

In globular protein systems, upper critical solution temperature (UCST) behavior is common, but lower critical solution temperature (LCST) phase transitions are rare. In addition, the temperature sensitivity of such systems is usually difficult to tune. Here we demonstrate that the charge state of globular proteins in aqueous solutions can alter their temperature-dependent phase behavior. We show a universal way to tune the effective protein interactions and induce both UCST and LCST-type transitions in the system using trivalent salts. We provide a phase diagram identifying LCST and UCST regimes as a function of protein and salt concentrations. We further propose a model based on an entropy-driven cation binding mechanism to explain the experimental observations.

Graphical abstract: Unification of lower and upper critical solution temperature phase behavior of globular protein solutions in the presence of multivalent cations

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Article information


Submitted
26 Nov 2019
Accepted
27 Jan 2020
First published
28 Jan 2020

Soft Matter, 2020, Advance Article
Article type
Paper

Unification of lower and upper critical solution temperature phase behavior of globular protein solutions in the presence of multivalent cations

N. Begam, O. Matsarskaia, M. Sztucki, F. Zhang and F. Schreiber, Soft Matter, 2020, Advance Article , DOI: 10.1039/C9SM02329A

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